Revealing the ‘obscurin’: mapping the path to new discovery with the phosphoproteome

Revealing the ‘obscurin’: mapping the path to new discovery with the phosphoproteome
Waskiw‐Ford, Marcus; Fung, Hugo J. W.; Gavel, Erica; Ivanisevic, Olivera; Malowany, Julia M.; Rosenblat, Michael
2018-01-15 00:00:00
Skeletal muscle is a vital tissue for health and functionality and is constantly ‘turning over’ through the reciprocal processes of protein synthesis and protein breakdown. Exercise markedly increases protein turnover as a means to repair and remodel the composition of skeletal muscle. However, the mechanisms by which the mechanical stimulus of exercise is converted into the biochemical signals that elicit changes in protein turnover remain incompletely understood.Over the past decades, research has focused on a network of proteins within the mammalian target of rapamycin (mTOR) signalling cascade, which is a pathway intimately linked to protein turnover via its dual regulation of mRNA translation (i.e. protein synthesis) and proteolysis (i.e. protein breakdown). The traditional top‐down approach to study this pathway involves western blots to estimate the activity of known kinases (via changes in phosphorylation) following the application of an external stimulus (exercise, nutrition, etc.). This method has significantly advanced our understanding of a number of intracellular signalling processes associated with protein turnover, but given its general reliance on established proteins the potential for discovery via this approach is arguably nearing its limit. Novel ‘omics’ methods (e.g. proteomics and the recent phosphoproteomics) take a non‐targeted, bottom‐up approach, which involves assessing vast
http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.pngThe Journal of PhysiologyWileyhttp://www.deepdyve.com/lp/wiley/revealing-the-obscurin-mapping-the-path-to-new-discovery-with-the-HHqffq0Njt

Revealing the ‘obscurin’: mapping the path to new discovery with the phosphoproteome

Abstract

Skeletal muscle is a vital tissue for health and functionality and is constantly ‘turning over’ through the reciprocal processes of protein synthesis and protein breakdown. Exercise markedly increases protein turnover as a means to repair and remodel the composition of skeletal muscle. However, the mechanisms by which the mechanical stimulus of exercise is converted into the biochemical signals that elicit changes in protein turnover remain incompletely understood.Over the past decades, research has focused on a network of proteins within the mammalian target of rapamycin (mTOR) signalling cascade, which is a pathway intimately linked to protein turnover via its dual regulation of mRNA translation (i.e. protein synthesis) and proteolysis (i.e. protein breakdown). The traditional top‐down approach to study this pathway involves western blots to estimate the activity of known kinases (via changes in phosphorylation) following the application of an external stimulus (exercise, nutrition, etc.). This method has significantly advanced our understanding of a number of intracellular signalling processes associated with protein turnover, but given its general reliance on established proteins the potential for discovery via this approach is arguably nearing its limit. Novel ‘omics’ methods (e.g. proteomics and the recent phosphoproteomics) take a non‐targeted, bottom‐up approach, which involves assessing vast

Journal

The Journal of Physiology
– Wiley

Published: Jan 15, 2018

Keywords: ; ;

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References

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Resistance training‐induced changes in integrated myofibrillar protein synthesis are related to hypertrophy only after attenuation of muscle damage